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Literature summary extracted from

  • Kurzban, G.P.; Howarth, J.; Palmer, G.; Strobel, H.W.
    NADPH-cytochrome P-450 reductase. Physical properties and redox behavior in the absence of the FAD moiety (1990), J. Biol. Chem., 265, 12272-12279.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.6.2.4 stable to multiple freeze-thaw cycles, FAD-depleted enzyme Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.2.4 cytoplasm
-
Rattus norvegicus 5737
-
1.6.2.4 microsome
-
Rattus norvegicus
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.4 Rattus norvegicus
-
Sprague-Dawley strain
-
1.6.2.4 Rattus norvegicus Sprague-Dawley
-
Sprague-Dawley strain
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.4 FAD-depleted enzyme Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.2.4 liver phenobarbital-treated animals Rattus norvegicus
-

Storage Stability

EC Number Storage Stability Organism
1.6.2.4 4°C or room temperature, at both low and high ionic strength, in the presence or absence of NADP, FAD-depleted enzyme Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.4 2 ferricytochrome c + NADPH
-
Rattus norvegicus 2 ferrocytochrome c + NADP+ + H+
-
?
1.6.2.4 2 ferricytochrome c + NADPH
-
Rattus norvegicus Sprague-Dawley 2 ferrocytochrome c + NADP+ + H+
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.4 FAD
-
Rattus norvegicus
1.6.2.4 FMN
-
Rattus norvegicus